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Polyclonal Antibody Immunoprecipitation Regulation of Cell Proliferation

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Tensin 2 belongs to the Tensin family of cytoskeletal proteins that includes Tensin 1-3 and Cten, which couple integrins to the actin cytoskeleton (1). Tensin proteins contain SH2 and phosphotyrosine binding (PTB) domains, which enable interaction with diverse signaling molecules and proteins. Tensin family proteins play important roles in signal transduction, cell proliferation, and motility (2-5).Tensin 2 is localized to focal adhesions of various tissues with highest expression in the heart, kidney, and liver (6,7). Tensin 2 inhibits Akt/PKB signaling via a phosphatase tensin-type domain (8). However, Tensin 2 also mediates thrombopoietin/c-Mpl signaling, which promotes Akt signaling (9). Interaction with Tensin 2 is essential for the tumor suppressor function of Deleted in Cancer 1 (DLC1) (10-12).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Rab11a, Rab11b, and Rab25 are members of the Rab11 subfamily of small Ras-like GTPases. Unlike universally expressed Rab11, typical Rab25 expression appears to be limited to gastrointestinal mucosa, kidney, and lung (1). Rab25 can associate with apical recycling vesicles to help regulate apical vesicle trafficking (2,3). Research studies indicate that atypical Rab25 expression can be associated with various forms of cancer. Increased Rab25 expression is associated with aggressive growth in ovarian and breast cancer, where Rab25 may inhibit apoptosis and promote cancer cell proliferation and invasion through regulation of vesicle transport and cellular motility (4-7). Interaction between Rab25 and β1 integrin promotes vesicle-mediated transport of integrin to pseudopodial tip membranes, fostering the persistent invasion of tumor cells (8). Conversely, the reported loss of Rab25 expression in a number of breast cancer cases has an unclear effect on cancer pathogenesis (9).

$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Cytosolic phospholipase A2 (cPLA2) is a ubiquitously distributed enzyme that catalyzes the hydrolysis of the sn-2 acyl bond of glycerolipids to produce lysophospholipids and release arachidonic acid (1). cPLA2 has been implicated in diverse cellular responses such as mitogenesis, differentiation, inflammation and cytotoxicity (1). Calcium binding to the amino-terminal CalB domain of cPLA2 promotes the translocation of cPLA2 from cytosol to membrane, where cPLA2 cleaves arachidonic acid from natural membrane (2). Phosphorylation of cPLA2 by MAPK (p42/44 and p38) at Ser505 (3,4) and Ser727 (5) stimulates its catalytic activity.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Interferon regulatory factors (IRFs) comprise a family of transcription factors that function within the Jak/Stat pathway to regulate interferon (IFN) and IFN-inducible gene expression in response to viral infection (1). IRFs play an important role in pathogen defense, autoimmunity, lymphocyte development, cell growth, and susceptibility to transformation. The IRF family includes nine members: IRF-1, IRF-2, IRF-9/ISGF3γ, IRF-3, IRF-4 (Pip/LSIRF/ICSAT), IRF-5, IRF-6, IRF-7, and IRF-8/ICSBP. All IRF proteins share homology in their amino-terminal DNA-binding domains. IRF family members regulate transcription through interactions with proteins that share similar DNA-binding motifs, such as IFN-stimulated response elements (ISRE), IFN consensus sequences (ICS), and IFN regulatory elements (IRF-E) (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: RPA70 (HSSB, REPA1, RF-A, RP-A, p70) is a component of a heterotrimeric complex, composed of 70, 32/30 and 14 kDa subunits, collectively known as RPA. RPA is a single stranded DNA binding protein, whose DNA binding activity is believed to reside entirely in the 70 kDa subunit. The complex is required for almost all aspects of cellular DNA metabolism such as DNA replication (1-3), recombination, cell cycle and DNA damage checkpoints, and all major types of DNA repair including nucleotide excision, base excision, mismatch and double-strand break repairs (4-7). In response to genotoxic stress in eukaryotic cells, RPA has been shown to associate with the Rad9/Rad1/Hus1 (9-1-1) checkpoint complex (8). RPA is hyperphosphorylated upon DNA damage or replication stress by checkpoint kinases including ataxia telangiectasia mutated (ATM), ATM and Rad3-related (ATR), and DNA-dependent protein kinase (DNA-PK) (9-11). Phosphorylation of RPA32 occurs at serines 4, 8 and 33 (11). Hyperphosphorylation may alter RPA-DNA and RPA-protein interactions. In addition to the checkpoint partners, RPA interacts with a wide variety of protein partners, including proteins required for normal replication such as RCF, PCNA and Pol α, and also proteins involved in SV40 replication, such as DNA polymerase I and SV40 large T antigen (10,12).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Notch signaling is activated upon engagement of the Notch receptor with its ligands, the DSL (Delta, Serrate, Lag2) proteins of single-pass type I membrane proteins. The DSL proteins contain multiple EGF-like repeats and a DSL domain that is required for binding to Notch (1,2). Five DSL proteins have been identified in mammals: Jagged1, Jagged2, Delta-like (DLL) 1, 3 and 4 (3). Ligand binding to the Notch receptor results in two sequential proteolytic cleavages of the receptor by the ADAM protease and the γ-secretase complex. The intracellular domain of Notch is released and then translocates to the nucleus where it activates transcription. Notch ligands may also be processed in a way similar to Notch, suggesting a bi-directional signaling through receptor-ligand interactions (4-6).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: MEP50 (methylosome protein 50) is a component of the methylosome, a protein arginine methyltransferase complex that modifies specific arginine residues found in arginine- and glycine-rich regions of some spliceosomal Sm proteins. MEP50 is important for methylosome activity and may regulate the transfer of Sm proteins to the SMN (survival of motor neurons) complex, an early step in the assembly of U snRNPs. Both the methylosome and the SMN complex are essential for the assembly of spliceosomal snRNPs (1).MEP50 is a WD repeat protein that may provide an interface for multiple protein interactions between methylosome proteins. (1). It binds to JBP1, an arginine protein methyltransferase component of the methylosome. MEP50 has been shown to interact with CTD phosphatase FCP1 (CTDP1), a protein that may link the processes of transcriptional elongation and splicing (2), and with SUZ12, a polycomb group protein involved in transcriptional repression (3). JBP1 and MEP50 have also been reported to interact with the methyl-CpG binding protein complex MBD2/NuRD (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: MEP50 (methylosome protein 50) is a component of the methylosome, a protein arginine methyltransferase complex that modifies specific arginine residues found in arginine- and glycine-rich regions of some spliceosomal Sm proteins. MEP50 is important for methylosome activity and may regulate the transfer of Sm proteins to the SMN (survival of motor neurons) complex, an early step in the assembly of U snRNPs. Both the methylosome and the SMN complex are essential for the assembly of spliceosomal snRNPs (1).MEP50 is a WD repeat protein that may provide an interface for multiple protein interactions between methylosome proteins. (1). It binds to JBP1, an arginine protein methyltransferase component of the methylosome. MEP50 has been shown to interact with CTD phosphatase FCP1 (CTDP1), a protein that may link the processes of transcriptional elongation and splicing (2), and with SUZ12, a polycomb group protein involved in transcriptional repression (3). JBP1 and MEP50 have also been reported to interact with the methyl-CpG binding protein complex MBD2/NuRD (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Cytosolic phospholipase A2 (cPLA2) is a ubiquitously distributed enzyme that catalyzes the hydrolysis of the sn-2 acyl bond of glycerolipids to produce lysophospholipids and release arachidonic acid (1). cPLA2 has been implicated in diverse cellular responses such as mitogenesis, differentiation, inflammation and cytotoxicity (1). Calcium binding to the amino-terminal CalB domain of cPLA2 promotes the translocation of cPLA2 from cytosol to membrane, where cPLA2 cleaves arachidonic acid from natural membrane (2). Phosphorylation of cPLA2 by MAPK (p42/44 and p38) at Ser505 (3,4) and Ser727 (5) stimulates its catalytic activity.

$303
100 µl
$717
300 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Flow Cytometry, Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: CrkL, a 39 kDa adaptor protein, has a key regulatory role in hematopoietic cells. CrkL has one SH2 and two SH3 domains, with 60% homology to CrkII (1). The amino-terminal SH3 domain of CrkL binds proteins such as C3G, SOS, PI3K, c-Abl and BCR/Abl. The SH2 domain of CrkL can bind to tyrosine-phosphorylated proteins such as Cbl, HEF1, CAS and paxillin (2,3). CrkL is involved in various signaling cascades initiated by different cytokines and growth factors. The biological outcomes of the Crk-activated signal transduction include the modulation of cell adhesion, cell migration and immune cell responses (4). CrkL is a prominent substrate of the BCR/Abl oncoprotein in chronic myelogenous leukemia and binds to both BCR/Abl and c-Abl (5). CrkL is prominently and constitutively tyrosine phosphorylated in CML neutrophils and is not phosphorylated in normal neutrophils. Moreover, stimulation of normal neutrophils with cytokines and agonists does not induce tyrosine phosphorylation of this protein (6), indicating that it may be a useful target for therapeutic intervention or as a disease marker. Tyr207 in CrkL is the BCR/Abl phosphorylation site (7).

$303
100 µl
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Immunofluorescence (Frozen), Immunoprecipitation, Western Blotting

Background: The μ-opioid receptor (MOR) belongs to the superfamily of G-protein-coupled receptors. MOR mediates the analgesic and rewarding effects of morphine and other opiates as well as the actions of several endogenous opioid peptides (1). Upon binding to its ligands, this Gi-coupled receptor inactivates adenylyl cyclase (1) and activates a variety of G-beta-gamma-dependent pathways including the MAPK and the PI3K/Akt cascades (2,3). Trafficking of these receptors to and from the plasma membrane and their desensitization play a significant role in morphine tolerance (4,5). As with other GPCRs, these processes are modulated by phosphorylation at diverse sites within intracellular domains (6). Among other sites, agonist-specific phosphorylation of serine 375 in mouse (serine 377 in human) MOR is essential for its internalization (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: The Silent Information Regulator (Sir2) family of genes is a highly conserved group of genes that encode nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylases, also known as class III histone deacetylases. The first discovered and best characterized of this family is Saccharomyces cerevisiae Sir2, which is involved in silencing of mating type loci, telomere maintenance, DNA damage response, and cell aging (1). SirT6, a mammalian homolog of Sir2, is a nuclear, chromatin-associated protein that promotes the normal maintenance of genome integrity mediated by the base excision repair (BER) pathway (2-4). The BER pathway repairs single-stranded DNA lesions that arise spontaneously from endogenous alkylation, oxidation, and deamination events. SirT6 deficient mice show increased sensitivity to DNA-damaging agents, including the alkylating agents MMS and H2O2 (2). In addition, these mice show genome instability with increased frequency of fragmented chromosomes, detached centromeres, and gaps (2). SirT6 may regulate the BER pathway by deacetylating DNA Polβ or other core components of the pathway (2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein kinase R (PKR) is transcriptionally induced by interferon and activated by double-stranded RNA (dsRNA). PKR inhibits translation initiation through phosphorylation of the α subunit of the initiation factor eIF2 (eIF2α) and also controls the activation of several transcription factors, such as NF-κB, p53, and the Stats. In addition, PKR mediates apoptosis induced by many different stimuli, such as LPS, TNF-α, viral infection, and serum starvation (1,2). Activation of PKR by dsRNA results in PKR dimerization and autophosphorylation of Thr446 and Thr451 in the activation loop. Substitution of threonine for alanine at position 451 completely inactivated PKR, while a mutant with a threonine to alanine substitution at position 446 was partially active (3). Research studies have implicated PKR activation in the pathologies of neurodegenerative diseases, including Alzheimer's disease (4,5).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TTK (Mps1, PYT) is a cell cycle regulated dual specificity kinase present in rapidly proliferating tissues and cell lines (1-3). TTK localizes to kinetochores and centromeres and is an essential component of the mitotic spindle checkpoint as well as centrosome duplication (4-6). The mitotic checkpoint inhibits entry into anaphase until all chromosomes are attached to the spindle; inhibition of this process leads to genomic instability and tumorigenesis. Phosphorylation of the BLM helicase at Ser144 by TTK maintains chromosome stability during mitosis (7). Small molecule inhibitors of TTK can block the spindle checkpoint response, thereby making TTK a potential therapeutic target (8,9).TTK also participates in the DNA damage response by directly phosphorylating and activating the cell cycle checkpoint kinase Chk2 at Thr68. Two targets phosphorylated by Chk2 are the cell cycle phosphatase cdc25 and the transcription factor p53. Inactivation of cdc25 phosphatase results in the accumulation of inactive cyclin B and cell cycle arrest following DNA damage. Phosphorylation of p53 by active Chk2 stabilizes the transcription factor and promotes cell cycle arrest and apoptosis in response to DNA damage (10).

$111
20 µl
$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein ubiquitination and deubiquitination is a reversible process catalyzed by ubiquitinating enzymes (UBEs) and deubiquitinating enzymes (1,2). Deubiquitinating enzymes (DUBs) function as ubiquitin-specific proteases and can be divided into five subfamilies based on catalytic domain structure. At least 14 members of the JAMM ubiquitin protease subfamily have been identified, including signal transducing adaptor molecule (STAM) binding protein (3). STAM-binding protein (STAMBP or AMSH) is an endosomal DUB that preferentially displays ubiquitin isopeptidase activity toward K63-linked chains, which is critically dependent upon its interaction with STAM (4,5). STAMBP interacts with the STAM adaptor protein and becomes integrated into the multivesicular body sorting machinery to help regulate endosomal trafficking and receptor tyrosine kinase stability by deubiquitining target proteins (4,6). Evidence indicates that endosomal STAMBP antagonizes the ubiquitin-dependent trafficking of EGFR to the lysosomal compartment (7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: BAP1 (BRCA1-Associated Protein 1) was originally identified as a BRCA1 associated, nuclear localized ubiquitin hydrolase that suppresses cell growth (1). The protein belongs to the UCH family of deubiquitinases, with a UCH domain in its N-terminal segment and a BRCA1 interaction domain as well as a nuclear localization signal in its C-terminal segment (1). Frequent gene locus rearrangement, deletion and null mutation of BAP1 have been found in lung and breast cancers (1,2). Mutation analysis in vivo in cancer cell line survival and in animal tumorigenesis indicate that both the deubiquitinase activity and the nuclear localization signal are required for BAP1 function as a tumor suppressor (3). BAP1 does not have direct deubiquitination activity towards the autoubiquitinyled BRCA1/BARD1 E3 complex (4), but its interaction with BARD1 inhibits BRCA1/BARD1 E3 activity by interfering with the compex dimerization process (5). In addition to its interaction with BRCA1/BARD1, BAP1 has also been shown to interact with and deubiquitinylate HCF-1, thereby controlling its stability (6).Phosphorylation of Ser592 on BAP1 was identified at Cell Signaling Technology (CST) using PhosphoScan®, CST's LC-MS/MS platform for phosphorylation site discovery (7).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Bone morphogenetic proteins (BMPs) constitute a large family of signaling molecules that regulate a wide range of critical processes including morphogenesis, cell-fate determination, proliferation, differentiation, and apoptosis (1,2). BMP receptors are members of the TGF-β family of Ser/Thr kinase receptors. Ligand binding induces multimerization, autophosphorylation, and activation of these receptors (3-5). They subsequently phosphorylate Smad1 at Ser463 and Ser465 in the carboxy-terminal motif SSXS, as well as Smad5 and Smad9 (Smad8) at their corresponding sites. These phosphorylated Smads dimerize with the coactivating Smad4 and translocate to the nucleus, where they stimulate transcription of target genes (5).MAP kinases and CDKs 8 and 9 phosphorylate residues in the linker region of Smad1, including Ser206. The phosphorylation of Ser206 recruits Smurf1 to the linker region and leads to the degradation of Smad1 (6). Phosphorylation of this site also promotes Smad1 transcriptional action by recruiting YAP to the linker region (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The aldehyde dehydrogenase family is a large group of enzymes that catalyze the oxidization of aldehydes into carboxylic acids (1). Aldehyde Dehydrogenase 1A2 (ALDH1A2, RALHD2) is among a group of aldehyde dehydrogenases that catalyze the metabolism of retinaldehyde into retinoic acid (RA), which plays a critically important signaling role in animal development (2). Research studies have shown that ALDH1A2 also plays a role postnatally in modulating the effects of RA signaling on immune cell function (3-5). In one example using a genetic mouse model, it was shown that ALDH1A2-dependent RA signaling was a downstream mediator of NOTCH-dependent T cell differentiation (6).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Etk, also known as BMX, is a member of the Bruton's tyrosine kinase (Btk) family (1). It is expressed in a variety of hematopoietic, epithelial and endothelial cells. Etk, like other Btk family members, contains a pleckstrin homology (PH) domain and Src homology SH3 and SH2 domains. It participates in multiple signal transduction pathways (2). Phosphorylation of Tyr566 by Src kinase is required for activation of Etk in vivo (3). In endothelial and epithelial cells, Etk is regulated by FAK through phosphorylation at Tyr40 (4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein arginine N-methyltransferase 4 (PRMT4), also known as coactivator-associated arginine methyltransferase 1 (CARM1), is a member of the protein arginine N-methyltransferase (PRMT) family of proteins, which catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (1). There are two types of PRMT proteins. While both types catalyze the formation of mono-methyl arginine, type I PRMTs (PRMT1, 3, 4 and 6) add an additional methyl group to produce asymmetric di-methyl arginine and type II PRMTs (PRMT 5 and 7) produce symmetric di-methyl arginine (1). Mono-methyl arginine, but not di-methyl arginine, can be converted to citrulline through deimination performed by enzymes such as PADI4 (2). Most of the PRMTs methylate arginine residues found within glycine-arginine rich (GAR) domains of proteins, such as RGG, RG and RXR repeats (1). However, PRMT4/CARM1 and PRMT5 instead methylate arginine residues within PGM (proline-, glycine-, methionine-rich) motifs (3). PRMT4 methylates Arg2, 17 and 26 of histone H3 and cooperates synergistically with p300/CBP and p160 coactivators to enhance transcriptional activation by nuclear receptor proteins (4). In addition, PRMT4 methylates many non-histone proteins, including transcriptional coactivators (p300/CBP, SRC-3) (5,6,7,8), splicing factors (SmB, CA150, SAP49, UIC) (3), RNA binding proteins (PABP1, Sam68, HuD, HuR) (9,10,11), and thymocyte cyclic AMP-regulated phosphoprotein (TARPP) (12), suggesting additional functions in transcriptional regulation, mRNA processing and thymocyte maturation. Methylation of the splicing factor CA150 by PRMT4 facilitates an interaction with the Tudor domain of SMN, suggesting a role for PRMT4 in spinal muscular atrophy (3).